Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein

M. Robotta; C. Hintze; S. Schildknecht; Niels Zijlstra; C. Jungst; C. Karreman; M. Huber; M. Leist; Vinod Subramaniam; M. Drescher

doi:10.1021/bi300357a

Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein

M. Robotta, C. Hintze, S. Schildknecht, Niels Zijlstra, C. Jungst, C. Karreman, M. Huber, M. Leist, Vinod Subramaniam, M. Drescher

Research output: Contribution to journal › Article › Academic › peer-review

24 Citations (Scopus)

Abstract

α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform

Original language	Undefined
Pages (from-to)	3960-3962
Number of pages	3
Journal	Biochemistry (USA)
Volume	51
Issue number	19
DOIs	https://doi.org/10.1021/bi300357a
Publication status	Published - 2012

Keywords

METIS-289434
IR-84730

Access to Document

10.1021/bi300357a

Cite this

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title = "Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein",

abstract = "α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson{\textquoteright}s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform",

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author = "M. Robotta and C. Hintze and S. Schildknecht and Niels Zijlstra and C. Jungst and C. Karreman and M. Huber and M. Leist and Vinod Subramaniam and M. Drescher",

year = "2012",

doi = "10.1021/bi300357a",

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T1 - Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein

AU - Robotta, M.

AU - Hintze, C.

AU - Schildknecht, S.

AU - Zijlstra, Niels

AU - Jungst, C.

AU - Karreman, C.

AU - Huber, M.

AU - Leist, M.

AU - Subramaniam, Vinod

AU - Drescher, M.

PY - 2012

Y1 - 2012

N2 - α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform

AB - α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform

KW - METIS-289434

KW - IR-84730

U2 - 10.1021/bi300357a

DO - 10.1021/bi300357a

M3 - Article

VL - 51

SP - 3960

EP - 3962

JO - Biochemistry (USA)

JF - Biochemistry (USA)

SN - 0006-2960

IS - 19

ER -